Author: Nila Roy Choudhury; Gregory Heikel; Maryia Trubitsyna; Peter Kubik; Jakub Stanislaw Nowak; Shaun Webb; Sander Granneman; Christos Spanos; Juri Rappsilber; Alfredo Castello; Gracjan Michlewski
Title: RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination Document date: 2017_10_9
ID: ifla4aix_8
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https: //doi.org/10.1101/200410 doi: bioRxiv preprint Finally, we wanted to check if TRIM25ΔRBD could fold correctly and form multimeric complexes. To test this, we overexpressed T7-tagged TRIM25 with EGFP-tagged TRIM25 (with or without the Δ RBD mutation) in TRIM25 KO cells and performed anti-T7 coimmunoprecipitation (co-IP) assays (Fig. 2a) . Our resu.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https: //doi.org/10.1101/200410 doi: bioRxiv preprint Finally, we wanted to check if TRIM25ΔRBD could fold correctly and form multimeric complexes. To test this, we overexpressed T7-tagged TRIM25 with EGFP-tagged TRIM25 (with or without the Δ RBD mutation) in TRIM25 KO cells and performed anti-T7 coimmunoprecipitation (co-IP) assays (Fig. 2a) . Our results showed that both wild-type T7-TRIM25 and T7-TRIM25ΔRBD could interact with EGFP-TRIM25 (Fig. 2a) . The control experiment revealed that the T7 antibody co-IPed T7-tagged but not EGFP-tagged TRIM25
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